Journal
FEBS LETTERS
Volume 589, Issue 19, Pages 2477-2486Publisher
WILEY
DOI: 10.1016/j.febslet.2015.08.029
Keywords
Elastin-like polypeptide; Intrinsically disordered protein; Phase transition; Biopolymer; Tandem repeat; Protein engineering
Funding
- NIGMS NIH HHS [R01 GM061232] Funding Source: Medline
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Elastin-like polypeptides (ELPs) are a class of stimuli-responsive biopolymers inspired by the intrinsically disordered domains of tropoelastin that are composed of repeats of the VPGXG pentapeptide motif, where X is a guest residue. They undergo a reversible, thermally triggered lower critical solution temperature (LCST) phase transition, which has been utilized for a variety of applications including protein purification, affinity capture, immunoassays, and drug delivery. ELPs have been extensively studied as protein polymers and as biomaterials, but their relationship to other disordered proteins has heretofore not been established. The biophysical properties of ELPs that lend them their unique material behavior are similar to the properties of many intrinsically disordered proteins (IDP). Their low sequence complexity, phase behavior, and elastic properties make them an interesting minimal artificial IDP, and the study of ELPs can hence provide insights into the behavior of other more complex IDPs. Motivated by this emerging realization of the similarities between ELPs and IDPs, this review discusses the biophysical properties of ELPs, their biomedical utility, and their relationship to other disordered polypeptide sequences. Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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